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Volumn 34, Issue SUPPL. C, 1998, Pages 1-9

Discovery and development of insulin lispro

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GLUCOSE; HUMAN INSULIN; INSULIN; INSULIN LISPRO; PROINSULIN; RECOMBINANT DNA; SOMATOMEDIN B; SOMATOMEDIN C; ZINC;

EID: 0031810210     PISSN: 16993993     EISSN: 16994019     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (13)

References (46)
  • 2
    • 50749118593 scopus 로고
    • The internal secretion of the pancreas
    • Banting, F.G., Best, C.H. The internal secretion of the pancreas. J Lab Clin Med 1922, 7: 251-66.
    • (1922) J Lab Clin Med , vol.7 , pp. 251-266
    • Banting, F.G.1    Best, C.H.2
  • 4
    • 0027421638 scopus 로고
    • Research, development, production, and safety of biosynthetic human insulin
    • Chance, R.E., Frank, B.H. Research, development, production, and safety of biosynthetic human insulin. Diabetes Care 1993, 16 (Suppl. 3): 133-42.
    • (1993) Diabetes Care , vol.16 , Issue.3 SUPPL. , pp. 133-142
    • Chance, R.E.1    Frank, B.H.2
  • 5
    • 84878676000 scopus 로고    scopus 로고
    • Better than mother nature
    • Ross, P.E. Better than mother nature. Forbes 1996, 150-4.
    • (1996) Forbes , pp. 150-154
    • Ross, P.E.1
  • 6
    • 0017345431 scopus 로고
    • Insulin today. the Banting Memorial Lecture 1976
    • Steiner, D.F. Insulin today. The Banting Memorial Lecture 1976. Diabetes 1977, 26: 322-40.
    • (1977) Diabetes , vol.26 , pp. 322-340
    • Steiner, D.F.1
  • 8
    • 0028092036 scopus 로고
    • Improving insulin therapy: Achievements and challenges
    • Galloway, J.A., Chance, R.E. Improving insulin therapy: Achievements and challenges. Horm Metab Res 1994, 26: 591-8.
    • (1994) Horm Metab Res , vol.26 , pp. 591-598
    • Galloway, J.A.1    Chance, R.E.2
  • 10
    • 0030606309 scopus 로고    scopus 로고
    • Mapping the functional surface of insulin by design: Structure and function of a novel A-chain analogue
    • Hua, Q.-X., Hu, S.-Q., Frank, B.H. et al. Mapping the functional surface of insulin by design: Structure and function of a novel A-chain analogue. J Mol Biol 1996, 264: 390-403.
    • (1996) J Mol Biol , vol.264 , pp. 390-403
    • Hua, Q.-X.1    Hu, S.-Q.2    Frank, B.H.3
  • 11
    • 0029986510 scopus 로고    scopus 로고
    • Solution structure of the superactive monomeric des[phe(B25)] human insulin mutant: Elucidation of the structural basis for the monomerization of des-[phe(B25)] insulin and the dimerization of native insulin
    • Jørgensen, A.M.M., Olsen, H.B., Balschmidt, P., Led, J.J. Solution structure of the superactive monomeric des[phe(B25)] human insulin mutant: Elucidation of the structural basis for the monomerization of des-[phe(B25)] insulin and the dimerization of native insulin. J Mol Biol 1996, 257: 684-99.
    • (1996) J Mol Biol , vol.257 , pp. 684-699
    • Jørgensen, A.M.M.1    Olsen, H.B.2    Balschmidt, P.3    Led, J.J.4
  • 12
    • 0031864008 scopus 로고    scopus 로고
    • Preclinical studies on insulin lispro
    • Llewelyn, J., Slieker, L.J., Zimmermann, J.L. Preclinical studies on insulin lispro. Drugs Today 1998, 34 (Suppl. C): 11-21.
    • (1998) Drugs Today , vol.34 , Issue.SUPPL. C , pp. 11-21
    • Llewelyn, J.1    Slieker, L.J.2    Zimmermann, J.L.3
  • 13
    • 0031836628 scopus 로고    scopus 로고
    • Pharmacokinetics and glucodynamics of insulin lispro
    • Heinemann, L., Woodworth, J.R. Pharmacokinetics and glucodynamics of insulin lispro. Drugs Today 1998, 34 (Suppl. C): 23-36.
    • (1998) Drugs Today , vol.34 , Issue.SUPPL. C , pp. 23-36
    • Heinemann, L.1    Woodworth, J.R.2
  • 14
    • 0031838586 scopus 로고    scopus 로고
    • Clinical Studies on insulin lispro
    • Anderson, J.H. Jr., Koivisto, V.A. Clinical Studies on insulin lispro. Drugs Today 1998, 34 (Suppl. C): 37-50.
    • (1998) Drugs Today , vol.34 , Issue.SUPPL. C , pp. 37-50
    • Anderson Jr., J.H.1    Koivisto, V.A.2
  • 16
    • 0026608746 scopus 로고
    • Biosynthetic human proinsulin. Review of chemistry, in vitro and in vivo receptor binding, animal and human pharmacology studies, and clinical trial experience
    • Galloway, J.A., Hooper, S.A., Spradlin, C.T. et al. Biosynthetic human proinsulin. Review of chemistry, in vitro and in vivo receptor binding, animal and human pharmacology studies, and clinical trial experience. Diabetes Care 1992, 15: 666-92.
    • (1992) Diabetes Care , vol.15 , pp. 666-692
    • Galloway, J.A.1    Hooper, S.A.2    Spradlin, C.T.3
  • 17
    • 0009713493 scopus 로고
    • Synthesis of insulin-like growth factor I through recombinant DNA techniques and selective chemical cleavage at tryptophan
    • Tam, J.P., Kaiser, E.T. (Eds.). Alan R. Liss: New York
    • DiMarchi, R., Long, H., Epp, J., Schoner, B., Belagaje, R. Synthesis of insulin-like growth factor I through recombinant DNA techniques and selective chemical cleavage at tryptophan. In: Synthetic Peptides: Approaches to Biological Problems. Tam, J.P., Kaiser, E.T. (Eds.). Alan R. Liss: New York 1989, 283-94.
    • (1989) Synthetic Peptides: Approaches to Biological Problems , pp. 283-294
    • Dimarchi, R.1    Long, H.2    Epp, J.3    Schoner, B.4    Belagaje, R.5
  • 18
    • 0023614302 scopus 로고
    • Recombinant human insulin-like growth factor II expressed in Escherichia coli
    • Furman, T.C., Epp, J., Hsiung, H.M. et al. Recombinant human insulin-like growth factor II expressed in Escherichia coli. Biotechnology 1987, 5: 1047-51.
    • (1987) Biotechnology , vol.5 , pp. 1047-1051
    • Furman, T.C.1    Epp, J.2    Hsiung, H.M.3
  • 20
    • 0025078913 scopus 로고
    • Monomeric insulins and their experimental and clinical implications
    • Brange, J., Owens, D.R., Kang, S., Vølund, A. Monomeric insulins and their experimental and clinical implications. Diabetes Care 1990, 13: 923-54.
    • (1990) Diabetes Care , vol.13 , pp. 923-954
    • Brange, J.1    Owens, D.R.2    Kang, S.3    Vølund, A.4
  • 21
    • 0002002069 scopus 로고
    • Synthesis of a fast-acting insulin based on structural homology with insulin-like growth factor I
    • Peptides. Chemistry and Biology. Smith, J.A., Rivier, J.E. (Eds.). ESCOM: Leiden
    • DiMarchi, R.D., Mayer, J.P., Fan, L. et al. Synthesis of a fast-acting insulin based on structural homology with insulin-like growth factor I. In: Peptides. Chemistry and Biology. Proceedings of the Twelfth American Peptide Symposium. Smith, J.A., Rivier, J.E. (Eds.). ESCOM: Leiden 1992, 26-8.
    • (1992) Proceedings of the Twelfth American Peptide Symposium , pp. 26-28
    • Dimarchi, R.D.1    Mayer, J.P.2    Fan, L.3
  • 22
    • 0001468029 scopus 로고
    • Soluble, prolonged-acting insulin derivatives. I. Degree of protraction and crystallizability of insulins substituted in the termini of the B-chain
    • Markussen, J., Hougaard, P., Ribel, U., Sørensen, A.R., Sorensen, E. Soluble, prolonged-acting insulin derivatives. I. Degree of protraction and crystallizability of insulins substituted in the termini of the B-chain. Protein Eng 1987, 1: 205-13.
    • (1987) Protein Eng , vol.1 , pp. 205-213
    • Markussen, J.1    Hougaard, P.2    Ribel, U.3    Sørensen, A.R.4    Sorensen, E.5
  • 23
    • 0000477832 scopus 로고
    • Soluble, prolonged-acting insulin derivatives. II. Degree of protraction and crystallizability of insulins substituted in positions A17, B8, B13, B27 and B30
    • Markussen, J., Diers, J., Engesgaard, A. et al. Soluble, prolonged-acting insulin derivatives. II. Degree of protraction and crystallizability of insulins substituted in positions A17, B8, B13, B27 and B30. Protein Eng 1987, 1: 215-23.
    • (1987) Protein Eng , vol.1 , pp. 215-223
    • Markussen, J.1    Diers, J.2    Engesgaard, A.3
  • 26
    • 77956751025 scopus 로고
    • Insulin: The structure in the crystal and its reflection in chemistry and biology
    • Blundell, T., Dodson, G., Hodgkin, D., Mercola, D. Insulin: The structure in the crystal and its reflection in chemistry and biology. Adv Protein Chem 1972, 26: 279-402.
    • (1972) Adv Protein Chem , vol.26 , pp. 279-402
    • Blundell, T.1    Dodson, G.2    Hodgkin, D.3    Mercola, D.4
  • 27
    • 0024280106 scopus 로고
    • The structure of 2Zn pig insulin crystals at 1.5 Å resolution
    • Baker, E.N., Blundell, T.L., Cutfield, J.F. et al. The structure of 2Zn pig insulin crystals at 1.5 Å resolution. Proc R Soc Lond B Biol Sci 1988, 319: 369-456.
    • (1988) Proc R Soc Lond B Biol Sci , vol.319 , pp. 369-456
    • Baker, E.N.1    Blundell, T.L.2    Cutfield, J.F.3
  • 29
    • 0018937820 scopus 로고
    • Role of zinc in insulin biosynthesis. Some possible zinc-insulin interactions in the pancreatic β-cell
    • Emdin, S.O., Dodson, G.G., Cutfield, J.M., Cutfield, S.M. Role of zinc in insulin biosynthesis. Some possible zinc-insulin interactions in the pancreatic β-cell. Diabetologia 1980, 19: 174-82.
    • (1980) Diabetologia , vol.19 , pp. 174-182
    • Emdin, S.O.1    Dodson, G.G.2    Cutfield, J.M.3    Cutfield, S.M.4
  • 30
    • 0015522139 scopus 로고
    • Conformation of proinsulin. A comparison of insulin and proinsulin self-association at neutral pH
    • Pekar, A.H., Frank, B.H. Conformation of proinsulin. A comparison of insulin and proinsulin self-association at neutral pH. Biochemistry 1972, 11: 4013-6.
    • (1972) Biochemistry , vol.11 , pp. 4013-4016
    • Pekar, A.H.1    Frank, B.H.2
  • 31
    • 0026078843 scopus 로고
    • Insulin association in neutral solutions studied by light scattering
    • Hvidt. S. Insulin association in neutral solutions studied by light scattering. Biophys Chem 1991, 39: 205-13.
    • (1991) Biophys Chem , vol.39 , pp. 205-213
    • Hvidt, S.1
  • 32
    • 0026698991 scopus 로고
    • Altering the association properties of insulin by amino acid replacement
    • Brems, D.N., Alter, L.A., Beckage, M.J. et al. Altering the association properties of insulin by amino acid replacement. Protein Eng 1992, 5: 527-33.
    • (1992) Protein Eng , vol.5 , pp. 527-533
    • Brems, D.N.1    Alter, L.A.2    Beckage, M.J.3
  • 33
    • 0028336707 scopus 로고
    • Preparation of an insulin with improved pharmacokinetics relative to human insulin through consideration of structural homology with insulin-like growth factor I
    • DiMarchi, R.D., Chance, R.E., Long, H.B., Shields, J.E., Slieker, L.J. Preparation of an insulin with improved pharmacokinetics relative to human insulin through consideration of structural homology with insulin-like growth factor I. Horm Res 1994, 41 (Suppl. 2): 93-6.
    • (1994) Horm Res , vol.41 , Issue.2 SUPPL. , pp. 93-96
    • Dimarchi, R.D.1    Chance, R.E.2    Long, H.B.3    Shields, J.E.4    Slieker, L.J.5
  • 34
    • 0344301735 scopus 로고
    • Human insulin analogs with rapid onset and short duration of action
    • Peptides. Chemistry and Biology. Smith, J.A., Rivier, J.E. (Eds.). ESCOM: Leiden
    • Long, H.B., Baker, J.C., Belagaje, R.M. et al. Human insulin analogs with rapid onset and short duration of action. In: Peptides. Chemistry and Biology. Proceedings of the Twelfth American Peptide Symposium. Smith, J.A., Rivier, J.E. (Eds.). ESCOM: Leiden 1992, 88-90.
    • (1992) Proceedings of the Twelfth American Peptide Symposium , pp. 88-90
    • Long, H.B.1    Baker, J.C.2    Belagaje, R.M.3
  • 35
    • 0004804348 scopus 로고
    • Manipulation of the position of proline in the B-chain produces monomeric insulins
    • Frank, B.H., Brems, D.N., Chance, R.E., DiMarchi, R.D., Shields, J.E. Manipulation of the position of proline in the B-chain produces monomeric insulins. Diabetes 1991, 40 (Suppl. 1): 423A.
    • (1991) Diabetes , vol.40 , Issue.1 SUPPL.
    • Frank, B.H.1    Brems, D.N.2    Chance, R.E.3    Dimarchi, R.D.4    Shields, J.E.5
  • 37
    • 8544226918 scopus 로고    scopus 로고
    • Modifications in the B10 and B26-30 regions of the B chain of human insulin alter affinity for the human IGF-I receptor more than for the insulin receptor
    • Slieker, L.J., Brooke, G.S., DiMarchi, R.D. et al. Modifications in the B10 and B26-30 regions of the B chain of human insulin alter affinity for the human IGF-I receptor more than for the insulin receptor. Diabetologia 1997, 40 (Suppl. 2): S54-61.
    • (1997) Diabetologia , vol.40 , Issue.2 SUPPL.
    • Slieker, L.J.1    Brooke, G.S.2    Dimarchi, R.D.3
  • 38
    • 0001065636 scopus 로고
    • Biological aspects of a new human insulin analog: [Lys(B28), Pro(B29)]-human insulin
    • Shaw, W.N., Su, K.S.E. Biological aspects of a new human insulin analog: [Lys(B28), Pro(B29)]-human insulin. Diabetes 1991, 40 (Suppl. 1): 464A.
    • (1991) Diabetes , vol.40 , Issue.1 SUPPL.
    • Shaw, W.N.1    Su, K.S.E.2
  • 40
    • 3843049754 scopus 로고
    • Using dog model for comparing time action of insulins af ter subcutaneous (s.c.) injection: Prediction of rapid onset of a new insulin analog [Lys(B28).Pro(B29)]-human insulin (KP)
    • Su, K.S., Campanale, K.M., Chance, R.E., Hoffmann, J.A. Using dog model for comparing time action of insulins af ter subcutaneous (s.c.) injection: Prediction of rapid onset of a new insulin analog [Lys(B28).Pro(B29)]-human insulin (KP). Pharm Res 1994, 11 (Suppl.): S-357.
    • (1994) Pharm Res , vol.11 , Issue.SUPPL.
    • Su, K.S.1    Campanale, K.M.2    Chance, R.E.3    Hoffmann, J.A.4
  • 45
    • 3843106456 scopus 로고
    • B29-human insulin (insulin lispro): Solution properties of a rapid-acting insulin
    • B29-human insulin (insulin lispro): Solution properties of a rapid-acting insulin. Diabetologia 1995, 38 (Suppl. 1): A189.
    • (1995) Diabetologia , vol.38 , Issue.1 SUPPL.
    • Frank, B.H.1    Baker, J.C.2    Bakaysa, D.L.3
  • 46
    • 84878732285 scopus 로고    scopus 로고
    • Insulin analogues: Designer insulins with improved characteristics for better patient care
    • Anderson, J.H. Jr., Wilke, T.S., DiMarchi, R.D., Chance, R.E. Insulin analogues: Designer insulins with improved characteristics for better patient care. Diabetes News 1996, XVII(2): 5-7.
    • (1996) Diabetes News , vol.17 , Issue.2 , pp. 5-7
    • Anderson Jr., J.H.1    Wilke, T.S.2    Dimarchi, R.D.3    Chance, R.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.